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Gene Review:

SCO4089 - valine dehydrogenase

Streptomyces coelicolor A3(2)

Synonyms: SCD25.25c, vdh

Tang, L. et al., Tang, L. et al., Navarrete, R.M. et al., Tang, L. et al., Turnbull, A.P. et al.

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Disease relevance of SCO4089

Expression of the Streptomyces coelicolor (Sc) valine (branched-chain amino acid) dehydrogenase-encoding gene (vdh) is regulated by valine, glucose and NH+4 at the transcriptional level [1].

High impact information on SCO4089

Analysis of the quaternary structure, substrate specificity, and catalytic mechanism of valine dehydrogenase [2].
This suggests that glucose repression of vdh and carbohydrate metabolism are due to the same mechanism in Sc, which involves glucose kinase [1].
The addition of the valine catabolite, propionate or isobutyrate, and introduction of the wild-type vdh gene back to each vdh::hyg mutant reversed the negative effect of the vdh::hyg mutation on spiramycin and tylosin production [3].
Expression of the vdh gene is repressed by > 25 mM ammonium ion or glucose but not by valine, glycerol, or maltose [4].
In minimal medium, VDH activity was repressed in the presence of glucose and NH4+, or glycerol and NH4+ or asparagine, and was induced by D- and L-valine [5].

References

Regulation of expression of the valine (branched-chain amino acid) dehydrogenase-encoding gene from Streptomyces coelicolor. Tang, L., Hutchinson, C.R. Gene (1995) [Pubmed]
Analysis of the quaternary structure, substrate specificity, and catalytic mechanism of valine dehydrogenase. Turnbull, A.P., Baker, P.J., Rice, D.W. J. Biol. Chem. (1997) [Pubmed]
Amino acid catabolism and antibiotic synthesis: valine is a source of precursors for macrolide biosynthesis in Streptomyces ambofaciens and Streptomyces fradiae. Tang, L., Zhang, Y.X., Hutchinson, C.R. J. Bacteriol. (1994) [Pubmed]
The genetic basis of precursor supply for the biosynthesis of macrolide and polyether antibiotics. Tang, L., Zhang, Y.X., Hutchinson, C.R. Ann. N. Y. Acad. Sci. (1994) [Pubmed]
Purification of an inducible L-valine dehydrogenase of Streptomyces coelicolor A3(2). Navarrete, R.M., Vara, J.A., Hutchinson, C.R. J. Gen. Microbiol. (1990) [Pubmed]

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